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Related Experiment Video

Updated: Mar 8, 2026

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome
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Improved surfaceome coverage with a label-free nonaffinity-purified workflow.

Tina Glisovic-Aplenc1,2, Saar Gill3, Lynn A Spruce4

  • 1Division of Oncology, Center for Childhood Cancer Research, The Children's Hospital of Philadelphia, Philadelphia, PA, USA.

Proteomics
|January 25, 2017
PubMed
Summary
This summary is machine-generated.

Researchers identified over 1900 cell surface proteins in leukemia cells, significantly expanding the known surfaceome. This breakthrough improves understanding of plasma membrane proteins and their roles in cellular functions.

Keywords:
GO termLabel-freeLeukemiaPlasma membraneSurfaceome

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Area of Science:

  • Proteomics
  • Cell Biology
  • Biochemistry

Background:

  • Plasma membrane (PM) proteins are crucial for cell homeostasis and communication.
  • The PM proteome is difficult to study due to low abundance and challenging isolation.
  • Standard methods often underrepresent PM proteins in analyses.

Purpose of the Study:

  • To develop an effective method for enriching and characterizing the plasma membrane proteome.
  • To identify a comprehensive set of cell surface proteins (surfaceome) in leukemia cells.
  • To overcome limitations of previous studies on the leukemia surfaceome.

Main Methods:

  • Utilized sucrose gradient ultracentrifugation for plasma membrane proteome enrichment.
  • Employed Gel-liquid chromatography-tandem mass spectrometry (GeLC-MS) for protein identification.
  • Applied bioinformatics tools to specifically select for PM/cell surface-associated proteins.

Main Results:

  • Identified over 1900 cell surface-associated proteins in a human acute myeloid leukemia cell line.
  • The identified surfaceome constitutes nearly 50% of all detected cellular proteins.
  • This represents a substantial increase in coverage compared to previous leukemia surfaceome studies.

Conclusions:

  • The developed method effectively enriches and characterizes the plasma membrane proteome.
  • This study significantly expands the catalog of known leukemia surface proteins.
  • The findings provide a deeper understanding of the leukemia surfaceome and its potential roles.